Theoretical and Natural Science
- The Open Access Proceedings Series for Conferences
Theoretical and Natural Science
Vol. 21, 20 December 2023
Open
Access | Article
Rabies’ proteins’ functions and future directions
* Author to whom correspondence should be addressed.
Abstract
The rabies virus, which mostly originates from the bite of a sick dog or cat and spreads, kills tens of thousands of people each year, and it is super lethal, with almost no one surviving the infection, s so, everyone is afraid of it. The main body of the rabies virus is bullet-shaped, and each combination of proteins in it is an innate destroyer. From the destruction of cells by the G and M proteins to the transcription of the P and L proteins in concert with each other, the precision, and division of labor of the rabies virus are obvious. Of these, the L protein is the key to the operation of everything, and this paper will explore the destruction of each protein, thereby stopping the spread of RABV. In particular, the possibility that the L protein, unlike rabies vaccines currently on the market, might be a future drug design idea by destroying the structure of RABV after the virus enters the cell. Keywords: Rabies, RABV, Protein Matching, L protein.
Keywords
rabies, RABV, protein matching, L protein.
References
1. “Rabies.” https://www.who.int/news-room/fact-sheets/detail/rabies
2. Davis, Benjamin M, et al. “Everything You Always Wanted to Know about Rabies Virus (but Were Afraid to Ask).” Ann. Rev. Virol.. 2015,
3. “Genus: Lyssavirus.”https://ictv.global/report/chapter/rhabdoviridae/rhabdoviridae/lyssavirus.
4. “What Is Rabies?” https://www.cdc.gov/rabies/about.html?CDC_AA_refVal=https%3A%2F%2Fwww.cdc.gov%2Frabies%2Ftransmission%2Fvirus.html.
5. Albertini, A. A. V., et al. “Structural Aspects of Rabies Virus Replication” Cell. Mol. Life Sci. 65 282, (2007).
6. Ben Khalifa, Youcef, et al. “The Matrix Protein of Rabies Virus Binds to RELAP43 to Modulate NF-ΚB-Dependent Gene Expression Related to Innate Immunity.” Sci. Rep., 21 (2016).
7. [7] Yang, Fanli. “Structural Analysis of Rabies Virus Glycoprotein Reveals PH-Dependent Conformational Changes and Interactions with a Neutralizing Antibody”, Cell host & microbe, 27(3): 441-453 (2020).
8. “Uniprot Website Fallback Message.” https://www.uniprot.org/uniprotkb/P03524/entry.
9. Mebatsion, T, et al. “Matrix Protein of Rabies Virus Is Responsible for the Assembly and Budding of Bullet-Shaped Particles and Interacts with the Transmembrane Spike Glycoprotein G.” J. Virol. 73, 242, (1999)
10. Yin, Juanbin, et al. “Research Advances on the Interactions between Rabies Virus Structural Proteins and Host Target Cells: Accrued Knowledge from the Application of Reverse Genetics Systems.” Viruses, 16, 2021,
11. “Uniprot Website Fallback Message.” https://www.uniprot.org/uniprotkb/P16285/entry.
12. “Uniprot Website Fallback Message.” https://www.uniprot.org/uniprotkb/A3F5L9/entry.
13. Ogino, Tomoaki, and Todd J Green. “Transcriptional Control and Mrna Capping by the GDP Polyribonucleotidyltransferase Domain of the Rabies Virus Large Protein.” Viruses, 1 (2019),
14. “Uniprot Website Fallback Message.” UniProt, https://www.uniprot.org/uniprotkb/P22363/entry.
15. Chenik, M, et al. “Mapping the Interacting Domains between the Rabies Virus Polymerase and Phosphoprotein.” J. Virol. (1998)
16. Green, Todd “Model of the Rabies Virus L Protein.” ModelArchive, (2020)
17. Nakagawa, Kento, et al. “Molecular Function Analysis of Rabies Virus RNA Polymerase L Protein by Using an L Gene-Deficient Virus.” J. Virol., U.S. National Library of Medicine, 2017.
Data Availability
The datasets used and/or analyzed during the current study will be available from the authors upon reasonable request.
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- Volume Title
- Proceedings of the 3rd International Conference on Biological Engineering and Medical Science
- ISBN (Print)
- 978-1-83558-215-2
- ISBN (Online)
- 978-1-83558-216-9
- Published Date
- 20 December 2023
- Series
- Theoretical and Natural Science
- ISSN (Print)
- 2753-8818
- ISSN (Online)
- 2753-8826
- DOI
- 10.54254/2753-8818/21/20230812
- Copyright
- 20 December 2023
- Open Access
- This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited